3zpd: Difference between revisions
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==Solution structure of the FimH adhesin carbohydrate-binding domain== | |||
<StructureSection load='3zpd' size='340' side='right' caption='[[3zpd]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zpd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_j96 Escherichia coli j96]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZPD FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zpd RCSB], [http://www.ebi.ac.uk/pdbsum/3zpd PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Uropathogenic Escherichia coli cause urinary tract infections by adhering to mannosylated receptors on the human urothelium via the carbohydrate-binding domain of the FimH adhesin (FimHL). Numerous alpha-d-mannopyranosides, including alpha-d-heptyl mannose (HM), inhibit this process by interacting with FimHL. To establish the molecular basis of the high-affinity HM binding, we solved the solution structure of the apo form and the crystal structure of the FimHL-HM complex. NMR relaxation analysis revealed that protein dynamics were not affected by the sugar binding, yet HM addition promoted protein dimerization, which was further confirmed by small-angle X-ray scattering. Finally, to address the role of Y48, part of the "tyrosine gate" believed to govern the affinity and specificity of mannoside binding, we characterized the FimHL Y48A mutant, whose conformational, dynamical, and HM binding properties were found to be very similar to those of the wild-type protein. | |||
Study of the Structural and Dynamic Effects in the FimH Adhesin upon alpha-d-Heptyl Mannose Binding.,Vanwetswinkel S, Volkov AN, Sterckx YG, Garcia-Pino A, Buts L, Vranken WF, Bouckaert J, Roy R, Wyns L, van Nuland NA J Med Chem. 2014 Feb 7. PMID:24476493<ref>PMID:24476493</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Buts, L | == References == | ||
[[Category: Nuland, N A.J van | <references/> | ||
[[Category: Vanwetswinkel, S | __TOC__ | ||
[[Category: Vranken, W F | </StructureSection> | ||
[[Category: Escherichia coli j96]] | |||
[[Category: Buts, L]] | |||
[[Category: Nuland, N A.J van]] | |||
[[Category: Vanwetswinkel, S]] | |||
[[Category: Vranken, W F]] | |||
[[Category: Bacterial adhesin]] | [[Category: Bacterial adhesin]] | ||
[[Category: Carbohydrate]] | [[Category: Carbohydrate]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Urinary tract infection]] | [[Category: Urinary tract infection]] | ||
